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| | ==Crystal structure of Pf-MAP(1-292)-C== | | ==Crystal structure of Pf-MAP(1-292)-C== |
| - | <StructureSection load='2dfi' size='340' side='right' caption='[[2dfi]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='2dfi' size='340' side='right'caption='[[2dfi]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2dfi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DFI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DFI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2dfi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DFI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xgm|1xgm]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">map ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dfi OCA], [https://pdbe.org/2dfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dfi RCSB], [https://www.ebi.ac.uk/pdbsum/2dfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dfi ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dfi OCA], [http://pdbe.org/2dfi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dfi RCSB], [http://www.ebi.ac.uk/pdbsum/2dfi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dfi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AMPM_PYRFU AMPM_PYRFU]] Removes the N-terminal methionine from nascent proteins. | + | [https://www.uniprot.org/uniprot/MAP2_PYRFU MAP2_PYRFU] Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).[HAMAP-Rule:MF_01975]<ref>PMID:9399590</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Aminopeptidase|Aminopeptidase]] | + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43587]] | + | [[Category: Large Structures]] |
| - | [[Category: Methionyl aminopeptidase]]
| + | |
| - | [[Category: Chon, H]]
| + | |
| - | [[Category: Kanaya, S]]
| + | |
| - | [[Category: Katagiri, Y]]
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| - | [[Category: Koga, Y]]
| + | |
| - | [[Category: Matsumura, H]]
| + | |
| - | [[Category: Takano, K]]
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| - | [[Category: Chameleon sequence]]
| + | |
| - | [[Category: Fusion protein]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Methionine aminopeptidase]]
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| - | [[Category: Pf-map]]
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| | [[Category: Pyrococcus furiosus]] | | [[Category: Pyrococcus furiosus]] |
| | + | [[Category: Chon H]] |
| | + | [[Category: Kanaya S]] |
| | + | [[Category: Katagiri Y]] |
| | + | [[Category: Koga Y]] |
| | + | [[Category: Matsumura H]] |
| | + | [[Category: Takano K]] |
| Structural highlights
Function
MAP2_PYRFU Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).[HAMAP-Rule:MF_01975][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Certain sequences, known as chameleon sequences, take both alpha- and beta-conformations in natural proteins. We demonstrate that a wild chameleon sequence fused to the C-terminal alpha-helix or beta-sheet in foreign stable proteins from hyperthermophiles forms the same conformation as the host secondary structure. However, no secondary structural formation is observed when the sequence is attached to the outside of the secondary structure. These results indicate that this sequence inherently possesses an ability to make either alpha- or beta-conformation, depending on the sequentially neighboring secondary structure if little other nonlocal interaction occurs. Thus, chameleon sequences take on a satellite state through contagion by the power of a secondary structure. We propose this "conformational contagion" as a new nonlocal determinant factor in protein structure and misfolding related to protein conformational diseases.
Conformational contagion in a protein: structural properties of a chameleon sequence.,Takano K, Katagiri Y, Mukaiyama A, Chon H, Matsumura H, Koga Y, Kanaya S Proteins. 2007 Aug 15;68(3):617-25. PMID:17510955[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tsunasawa S, Izu Y, Miyagi M, Kato I. Methionine aminopeptidase from the hyperthermophilic Archaeon Pyrococcus furiosus: molecular cloning and overexpression in Escherichia coli of the gene, and characteristics of the enzyme. J Biochem. 1997 Oct;122(4):843-50. PMID:9399590 doi:10.1093/oxfordjournals.jbchem.a021831
- ↑ Takano K, Katagiri Y, Mukaiyama A, Chon H, Matsumura H, Koga Y, Kanaya S. Conformational contagion in a protein: structural properties of a chameleon sequence. Proteins. 2007 Aug 15;68(3):617-25. PMID:17510955 doi:10.1002/prot.21451
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